Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
315
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Seq 36-60 Hetero dimer : IID00300 Complex
Region 5hky B 36-38 disorder
Region 5hky B 39-60 order
Region 5hkz B 36-59 order
Region 5hkz B 60-60 disorder
Seq 49-61 Hetero dimer : IID00300 Complex
Region 3bum A 49-51 disorder
Region 3bum A 52-60 order
Region 3bum A 61-61 disorder
Region 3ob1 A 49-49 disorder
Region 3ob1 A 50-59 order
Region 3ob1 A 60-60 disorder
Region 5hl0 B 54-59 order
Region 5hl0 B 60-60 disorder
Seq ProS predicted 50-60
Hetero dimer : IID00300 Complex
Region 5hky B 39-60 order
Region 5hkz B 36-59 order
Seq ProS predicted 50-60
Hetero dimer : IID00300 Complex
Region 3ob1 A 50-59 order
Region 3bum A 52-60 order
Region 5hl0 B 54-59 order
Prediction
Disorder 1-172,254-257,301-315
ProS 11-23,28-33,38-62,129-135,147-159,254-257,301-304
Disorder 1-40,49-173,231-237,245-247,302-315
Order 41-48,174-230,238-244,248-301
Function
Function in SwissProt
Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). Inhibits CBL/C-CBL-mediated EGFR ubiquitination (PubMed:17974561).
Biological Process
Diagram with PDB data
SPRY2/CBL Crystal structure of c-Cbl-TKB domain complexed with its binding motif in Sprouty2